Zinc Binding to Heliorhodopsin
Zinc Binding to Heliorhodopsin
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DOI：
10.1021/acs.jpclett.0c02383
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发表时间：
2020-10-15
影响因子：
5.7
通讯作者：
Kandori, Hideki
中科院分区：
文献类型：
--
作者：
Hashimoto, Masanori;Katayama, Kota;Kandori, Hideki
日光视紫红质（Heliorhodopsin，HeR）是最近发现的一个新的视紫红质家族，与动物和微生物视紫红质相比，其膜拓扑结构是倒置的，并且没有离子转运活性。HeRs的缓慢光循环表明了光传感器功能，尽管功能仍然未知。HeR不表现出一价阳离子或阴离子的特异性结合。尽管如此，在本研究中的ATR-FTIR光谱表明结合的锌2 + HeR从热等离子体目古菌（TaHeR）。的biding的Zn 2+到0.2 mM K-D是伴随着螺旋结构扰动，而不改变其颜色。即使离子特定的FTIR光谱观察到许多二价阳离子，只有螺旋结构扰动观察到锌+结合。对于HeR 48 C12获得了类似的结果。这些发现表明，可能的修改HeR功能的Zn 2+。
Heliorhodopsin (HeR), a recently discovered new rhodopsin family, has an inverted membrane topology compared to animal and microbial rhodopsins, and no ion-transport activity. The slow photocycle of HeRs suggests a light-sensor function, although the function remains unknown. HeRs exhibit no specific binding of monovalent cations or anions. Despite this, ATR-FTIR spectroscopy in the present study demonstrates binding of Zn2+ to HeR from Thermoplasmatales archaeon (TaHeR). The biding of Zn2+ to 0.2 mM K-d is accompanied by helical structural perturbations without altering its color. Even though ion-specific FTIR spectra were observed for many divalent cations, only helical structural perturbations were observed for Zn2+-binding. Similar results were obtained for HeR 48C12. These findings suggest a possible modification of HeR function by Zn2+.